Abstract
Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways. The regulatory aspect is conferred by a C-terminal cyclic nucleotide-binding domain (CNBD). We report resonance assignments of the CNBD of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magic-angle Spinning conditions. A secondary chemical shift analysis of the 141 residue protein suggests a three-dimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances.Electronic supplementary materialThe online version of this article (doi:10.1007/s12104-012-9363-4) contains supplementary material, which is available to authorized users.
Highlights
Channels regulated by cyclic nucleotides are key signalling proteins in several biological pathways
We report resonance assignments of the cyclic nucleotide-binding domain (CNBD) of a bacterial mlCNG channel obtained using 2D and 3D solid-state NMR under Magicangle Spinning conditions
A secondary chemical shift analysis of the 141 residue protein suggests a threedimensional fold seen in earlier X-ray and solution-state NMR work and points to spectroscopic polymorphism for a selected set of resonances
Summary
Cyclic nucleotides (cNMPs) are important secondary messenger molecules that mediate a multitude of processes by activating several different proteins in the signalling cascade. These proteins share a conserved regulatory protein unit referred to as cyclic nucleotide-binding domain. Upon binding cNMPs the regulatory CNBD renders the protein in an active conformation. The bacterial mlCNG channel displays distinctively different channel functioning property in being non-cooperative (Cukkemane et al 2007; Nimigean et al 2004). This provides a facile system in understanding the binding–gating relationship. We investigated the CNBD of mlCNG channel using solid-phase preparations paving the way for structural studies on the full-length channel
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